Xu Jun, Liu Shuangwei, Ren Yueming, You Yang, Wang Zhifang, Zhang Yongqiang, Zhu Xinjie, Hu Ping
College of Horticulture and Landscape Architecture, Henan Institute of Science and Technology, Xinxiang, Henan Province China.
College of Agricultural, Henan Institute of Science and Technology/Henan International Joint Laboratory of Plant Genetic Improvement and Soil Remediation, Xinxiang, 453003 Henan Province China.
3 Biotech. 2024 Sep;14(9):204. doi: 10.1007/s13205-024-04052-0. Epub 2024 Aug 18.
Heat shock protein 90 (HSP90) is important for many organisms, including plants. Based on the whole genome information, the gene number, gene structure, evolutionary relationship, protein structure, and active site of the HSP90 gene family in and were determined, and the expression of the gene under salt, and drought stresses in two rose varieties Wangxifeng and Sweet Avalanche were analyzed. Six and eight genes were identified from and , respectively. Phylogenetic analysis revealed that the analyzed genes were divided into two Groups and four subgroups (Classes 1a, 1b, 2a, and 2b). Although members within the same classes displayed highly similar gene structures, while the gene structures and conserved domains of Group 1 (Class 1a and 1b) and the Group 2 (Class 2a and 2b) are different. Tandem and segmental duplication genes were found in , but not in , perhaps explaining the difference in gene quantity in the two analyzed species. Analysis of cis-acting elements revealed abundant abiotic stress, photolight-response, and hormone-response elements in HSP90s. qRT-PCR analysis suggested that , and in Sweet Avalanche and Wangxifeng varieties played important regulatory roles under salt and drought stress. The analysis of protein structure and active sites indicate that the potential different roles of , , and in salt and drought stresses may come from the differences of corresponding protein structures and activation sites. These data will provide information for the breeding of rose varieties with high stress resistance.
The online version contains supplementary material available at 10.1007/s13205-024-04052-0.
热休克蛋白90（HSP90）对包括植物在内的许多生物体都很重要。基于全基因组信息，确定了[具体物种1]和[具体物种2]中HSP90基因家族的基因数量、基因结构、进化关系、蛋白质结构和活性位点，并分析了[具体基因]在两个玫瑰品种王希凤和甜蜜雪山的盐胁迫和干旱胁迫下的表达情况。分别从[具体物种1]和[具体物种2]中鉴定出6个和8个[具体基因]。系统发育分析表明，所分析的基因分为两组和四个亚组（1a类、1b类、2a类和2b类）。虽然同一类中的成员显示出高度相似的基因结构，但第1组（1a类和1b类）和第2组（2a类和2b类）的基因结构和保守结构域不同。在[具体物种1]中发现了串联和片段重复基因，但在[具体物种2]中未发现，这可能解释了两个分析物种中[具体基因]数量的差异。顺式作用元件分析表明，[具体物种1]的HSP90中存在丰富的非生物胁迫、光响应和激素响应元件。qRT-PCR分析表明，甜蜜雪山和王希凤品种中的[具体基因]在盐胁迫和干旱胁迫下发挥了重要的调节作用。蛋白质结构和活性位点分析表明，[具体基因]在盐胁迫和干旱胁迫中的潜在不同作用可能来自相应蛋白质结构和激活位点的差异。这些数据将为培育高抗逆性玫瑰品种提供信息。
在线版本包含可在10.1007/s13205-024-04052-0获取的补充材料。
